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Human HSP90 alpha N-terminal domain in complex with an Aminotriazoloquinazoline inhibitor

Source organism: Homo sapiens
Biochemical function: ATP-dependent protein folding chaperone
Biological process: protein folding
Cellular component: not assigned

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EC 3.6.4.10: Non-chaperonin molecular chaperone ATPase

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Systematic name:
ATP phosphohydrolase (polypeptide-polymerizing)
Alternative Name(s):
  • Molecular chaperone Hsc70 ATPase

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF13589
Domain description: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Occurring in:
  1. Heat shock protein HSP 90-alpha

InterPro InterPro annotations
IPR020575
Domain description: Heat shock protein Hsp90, N-terminal
Occurring in:
  1. Heat shock protein HSP 90-alpha
IPR003594
Domain description: Histidine kinase/HSP90-like ATPase
Occurring in:
  1. Heat shock protein HSP 90-alpha
IPR001404
Domain description: Heat shock protein Hsp90 family
Occurring in:
  1. Heat shock protein HSP 90-alpha
IPR036890
Domain description: Histidine kinase/HSP90-like ATPase superfamily
Occurring in:
  1. Heat shock protein HSP 90-alpha
IPR019805
Domain description: Heat shock protein Hsp90, conserved site
Occurring in:
  1. Heat shock protein HSP 90-alpha

Structure domain

CATH CATH domain
3.30.565.10
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Heat Shock Protein 90
Homology: Histidine kinase-like ATPase, C-terminal domain
Occurring in:
  1. Heat shock protein HSP 90-alpha
The deposited structure of PDB entry 4cwq contains 1 copy of CATH domain 3.30.565.10 (Heat Shock Protein 90) in Heat shock protein HSP 90-alpha. Showing 1 copy in chain A.

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